PPE_CAEEL
ID PPE_CAEEL Reviewed; 707 AA.
AC G5EBX9; C3JXD7; Q8MYR2;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Serine/threonine-protein phosphatase with EF-hands pef-1 {ECO:0000303|PubMed:9326663};
DE Short=CePPEF {ECO:0000303|PubMed:11312268};
DE EC=3.1.3.16 {ECO:0000255|RuleBase:RU004273};
DE AltName: Full=Phosphatase with EF hands 1 {ECO:0000312|WormBase:F23H11.8a};
GN Name=pef-1 {ECO:0000312|WormBase:F23H11.8a};
GN ORFNames=F23H11.8 {ECO:0000312|WormBase:F23H11.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAB82794.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=9326663; DOI=10.1073/pnas.94.21.11639;
RA Sherman P.M., Sun H., Macke J.P., Williams J., Smallwood P.M., Nathans J.;
RT "Identification and characterization of a conserved family of protein
RT serine/threonine phosphatases homologous to Drosophila retinal degeneration
RT C.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11639-11644(1997).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CALCIUM-BINDING, MYRISTOYLATION
RP AT GLY-2, PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF GLY-2 AND CYS-3.
RX PubMed=11312268; DOI=10.1074/jbc.m011712200;
RA Ramulu P., Nathans J.;
RT "Cellular and subcellular localization, N-terminal acylation, and calcium
RT binding of Caenorhabditis elegans protein phosphatase with EF-hands.";
RL J. Biol. Chem. 276:25127-25135(2001).
CC -!- FUNCTION: Probably acts as a protein phosphatase. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000255|RuleBase:RU004273};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000255|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P36873};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P36873};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11312268};
CC Lipid-anchor {ECO:0000269|PubMed:11312268}. Perikaryon
CC {ECO:0000269|PubMed:11312268}. Cell projection, dendrite
CC {ECO:0000269|PubMed:11312268}. Cell projection, axon
CC {ECO:0000269|PubMed:11312268}. Cell projection, cilium
CC {ECO:0000269|PubMed:11312268}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F23H11.8a};
CC IsoId=G5EBX9-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F23H11.8b};
CC IsoId=G5EBX9-2; Sequence=VSP_058324;
CC Name=c {ECO:0000312|WormBase:F23H11.8c};
CC IsoId=G5EBX9-3; Sequence=VSP_058325;
CC -!- TISSUE SPECIFICITY: Expression is restricted to neurons. Expressed in
CC AWB, AWC, AVA, AVB, AVX, BAG and URX neurons and in one tail neuron (at
CC protein level). {ECO:0000269|PubMed:11312268}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000255|RuleBase:RU004273}.
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DR EMBL; AF023454; AAB82794.1; -; mRNA.
DR EMBL; BX284603; CCD69949.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD69950.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD69954.1; -; Genomic_DNA.
DR PIR; T34072; T34072.
DR PIR; T42239; T42239.
DR RefSeq; NP_001022545.1; NM_001027374.2.
DR RefSeq; NP_001254836.1; NM_001267907.1. [G5EBX9-3]
DR RefSeq; NP_741091.1; NM_171080.4. [G5EBX9-1]
DR AlphaFoldDB; G5EBX9; -.
DR SMR; G5EBX9; -.
DR STRING; 6239.F23H11.8a; -.
DR iPTMnet; G5EBX9; -.
DR SwissPalm; G5EBX9; -.
DR EPD; G5EBX9; -.
DR PaxDb; G5EBX9; -.
DR PeptideAtlas; G5EBX9; -.
DR PRIDE; G5EBX9; -.
DR EnsemblMetazoa; F23H11.8a.1; F23H11.8a.1; WBGene00003969. [G5EBX9-1]
DR EnsemblMetazoa; F23H11.8b.1; F23H11.8b.1; WBGene00003969. [G5EBX9-2]
DR EnsemblMetazoa; F23H11.8b.2; F23H11.8b.2; WBGene00003969. [G5EBX9-2]
DR EnsemblMetazoa; F23H11.8c.1; F23H11.8c.1; WBGene00003969. [G5EBX9-3]
DR GeneID; 175257; -.
DR KEGG; cel:CELE_F23H11.8; -.
DR UCSC; F23H11.8a; c. elegans.
DR CTD; 175257; -.
DR WormBase; F23H11.8a; CE27999; WBGene00003969; pef-1. [G5EBX9-1]
DR WormBase; F23H11.8b; CE30662; WBGene00003969; pef-1. [G5EBX9-2]
DR WormBase; F23H11.8c; CE43732; WBGene00003969; pef-1. [G5EBX9-3]
DR eggNOG; KOG0377; Eukaryota.
DR GeneTree; ENSGT00940000169749; -.
DR InParanoid; G5EBX9; -.
DR OMA; ATHMLTM; -.
DR OrthoDB; 316811at2759; -.
DR PhylomeDB; G5EBX9; -.
DR PRO; PR:G5EBX9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003969; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR013235; PPP_dom.
DR InterPro; IPR012008; Ser/Thr-Pase_EF-hand_contain.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR PIRSF; PIRSF000912; PPEF; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection; Hydrolase;
KW Lipoprotein; Manganese; Membrane; Metal-binding; Myristate; Palmitate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11312268"
FT CHAIN 2..707
FT /note="Serine/threonine-protein phosphatase with EF-hands
FT pef-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436235"
FT DOMAIN 81..103
FT /note="IQ"
FT /evidence="ECO:0000255"
FT DOMAIN 546..581
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 629..664
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 669..704
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..518
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 318
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 369
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 465
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 684
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 686
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT BINDING 693
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:11312268"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11312268"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:11312268"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058324"
FT VAR_SEQ 17..81
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058325"
FT MUTAGEN 2
FT /note="G->A: Loss of palmitoylation and myristoylation
FT resulting in loss of association with the cell membrane.
FT Severe loss of axonal, dendritic and cilia localization in
FT AWC, AWB and BAG neurons."
FT /evidence="ECO:0000269|PubMed:11312268"
FT MUTAGEN 3
FT /note="C->S: Loss of palmitoylation resulting in loss of
FT association with the cell membrane. Moderate loss of
FT axonal, dendritic and cilia localization in AWC, AWB and
FT BAG neurons."
FT /evidence="ECO:0000269|PubMed:11312268"
SQ SEQUENCE 707 AA; 80330 MW; 1943CE218D0A7EF7 CRC64;
MGCGPSSGRQ NPSTELKKST RATTTTTSSS QRNNYNDNNQ NTSSSSGNKK ESSSSSKQHS
SKKSKKSNSK KNRSPSPQPQ LTIKSAILIQ KWYRRCEARL EARRRATWQI FTALEYAGEQ
DQLKLYDFFA DVIRAMAEEN GKGGVENGRN SPLMSALSHY AKPSLMDSEG ETVKKMLEDT
SPTNVDIDRN YKGPTLSLPL DKPQVAKMIE AFKVNKVLHP KYVLMILHEA RKIFKAMPSV
SRISTSISNQ VTICGDLHGK FDDLCIILYK NGYPSVDNPY IFNGDFVDRG GQSIEVLCVL
FALVIVDPMS IYLNRGNHED HIMNLRYGFI KELSTKYKDL STPITRLLED VFSWLPIATI
IDRDIFVVHG GISDQTEVSK LDKIPRHRFQ SVLRPPVNKG MESEKENSAV NVDEWKQMLD
IMWSDPKQNK GCWPNVFRGG GSYFGADITA SFLEKHGFRL LVRSHECKFE GYEFSHNNTC
LTVFSASNYY ETGSNRGAYV KFIGKSKQPH FVQYMASKTH RKSTLRERLG VVEESAVKEL
KEKLSSFHTD LQKEFEIMDI EKSGKLPILK WSDCVERITG LNLPWIALAP KVATLSEDGK
YVMYKEDRRI AQVGGTHAQE KDIVESLYRH KSTLETLFRF MDKDNSGQVS MKEFIDACEV
LGKYTKRPLQ TDYISQIAES IDFNKDGFID LNELLEAFRL VDRPLLR
